Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo. - Wikidata - awgldk - TriplyDB

Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo.

Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo.

http://www.wikidata.org/entity/Q30441600

about

Starch binding domain-containing protein 1/genethonin 1 is a novel participant in glycogen metabolism Laforin, the most common protein mutated in Lafora disease, regulates autophagy Laforin is required for the functional activation of malin in endoplasmic reticulum stress resistance in neuronal cells Structure of human PIR1, an atypical dual-specificity phosphatase Protein tyrosine phosphatases--from housekeeping enzymes to master regulators of signal transduction Autophagy and neurodegeneration Are there errors in glycogen biosynthesis and is laforin a repair enzyme?Structural basis for the glucan phosphatase activity of Starch Excess4 Structural and functional analysis of PTPMT1, a phosphatase required for cardiolipin synthesis Atomic Structure of Dual-Specificity Phosphatase 26, a Novel p53 Phosphatase Structure of the Arabidopsis Glucan Phosphatase LIKE SEX FOUR2 Reveals a Unique Mechanism for Starch Dephosphorylation Structural basis for 2'-phosphate incorporation into glycogen by glycogen synthase Phosphoglucan-bound structure of starch phosphatase Starch Excess4 reveals the mechanism for C6 specificity Voltage sensitive phosphatases: emerging kinship to protein tyrosine phosphatases from structure-function research The carbohydrate-binding domain of overexpressed STBD1 is important for its stability and protein-protein interactions Phosphate incorporation during glycogen synthesis and Lafora disease Early-onset Lafora body disease Loss of GABAergic cortical neurons underlies the neuropathology of Lafora disease PTG depletion removes Lafora bodies and rescues the fatal epilepsy of Lafora disease Conservation of the glucan phosphatase laforin is linked to rates of molecular evolution and the glucan metabolism of the organism Dimeric quaternary structure of human laforin.Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease.AMP-activated protein kinase phosphorylates R5/PTG, the glycogen targeting subunit of the R5/PTG-protein phosphatase 1 holoenzyme, and accelerates its down-regulation by the laforin-malin complex Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin Abnormal glycogen chain length pattern, not hyperphosphorylation, is critical in Lafora disease.Why pleiotropic interventions are needed for Alzheimer's disease.Protein degradation and quality control in cells from laforin and malin knockout mice.Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity The laforin-malin complex, involved in Lafora disease, promotes the incorporation of K63-linked ubiquitin chains into AMP-activated protein kinase beta subunits.Genetic depletion of the malin E3 ubiquitin ligase in mice leads to lafora bodies and the accumulation of insoluble laforin Insights into the mechanism of polysaccharide dephosphorylation by a glucan phosphatase Minireview: hey U(PS): metabolic and proteolytic homeostasis linked via AMPK and the ubiquitin proteasome system.Dimerization of Vaccinia virus VH1 is essential for dephosphorylation of STAT1 at tyrosine 701.Dimerization of the glucan phosphatase laforin requires the participation of cysteine 329.Glycogen phosphomonoester distribution in mouse models of the progressive myoclonic epilepsy, Lafora disease.Expression, purification and characterization of soluble red rooster laforin as a fusion protein in Escherichia coli.The laforin-malin complex negatively regulates glycogen synthesis by modulating cellular glucose uptake via glucose transporters.Laforin, a dual-specificity phosphatase involved in Lafora disease, is phosphorylated at Ser25 by AMP-activated protein kinase.Laforin, a protein with many faces: glucan phosphatase, adapter protein, et alii.Neurodegeneration and functional impairments associated with glycogen synthase accumulation in a mouse model of Lafora disease

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P2860

Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo.

http://www.wikidata.org/entity/Q30441600

description

2007 nî lūn-bûn

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2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2007 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

@wuu

name

Laforin is a glycogen phosphat ...... orylation of glycogen in vivo.

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Laforin is a glycogen phosphat ...... orylation of glycogen in vivo.

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type

label

Laforin is a glycogen phosphat ...... orylation of glycogen in vivo.

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Laforin is a glycogen phosphat ...... orylation of glycogen in vivo.

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prefLabel

Laforin is a glycogen phosphat ...... orylation of glycogen in vivo.

@ast

Laforin is a glycogen phosphat ...... orylation of glycogen in vivo.

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PNAS.0707952104

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Laforin is a glycogen phosphat ...... horylation of glycogen in vivo

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P2093

Alexander V Skurat

http://www.w3.org/2001/XMLSchema#string

Berge A Minassian

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Jean-Marie Girard

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Julie Turnbull

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Peter J Roach

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Vincent S Tagliabracci

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Wei Wang

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Xiaochu Zhao

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P2860

Myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate

Glycogen and its Metabolism

Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin.

The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B

Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates

Targeted disruption of the Epm2a gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioral response in mice

Glycogen and related polysaccharides inhibit the laforin dual-specificity protein phosphatase

Epm2a suppresses tumor growth in an immunocompromised host by inhibiting Wnt signaling

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19262-19266

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10.1073/PNAS.0707952104

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49

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104

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Antonio V Delgado-Escueta

Anna A. Depaoli-Roach

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2007-11-26T00:00:00Z

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5807880

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18040046

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phosphorylation

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2148278

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